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The Latest in Biopharm Discovery, Development, and Bioprocessing

Pall ForteBio systems have become indispensable tools at biopharmaceutical companies worldwide, resulting in a steady stream of scientific publications and presentations. This online resource will help you stay current on the latest studies featuring data from the Octet® and BLItz® systems. Fresh publications and presentations are captured as they become available, and can be browsed by application area or pinpointed by keyword search.

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  • H5N1 Vaccine-Elicited Memory B Cells Are Genetically Constrained by the IGHV Locus in the Recognition of a Neutralizing Epitope in the Hemagglutinin Stem
    Wheatley A, et al., J Immunol, 195(2):602-10, 2015
    Although it is becoming evident by the recent research that viral hemagglutinin (HA) could be the target for broadly neutralizing antibody responses, the frequency and phenotype of HA stem-specific B cells in vivo are yet to be revealed. This article focuses on HA stem-specific B cell responses following H5N1 vaccination and explains the re-expansion of memory B cells specific for stem epitopes. The kinetic characterization of binding between mAbs and HA were investigated using a Pall ForteBio Octet HTX system equipped with Streptavidin Biosensor probes. Biotinylated HA-trimers captured on to Streptavidin probes were used to screen against Fab of mAbs.


  • Heat Shock Protein 90 Mediates the Apoptosis and Autophage in Nicotinic-Mycoepoxydiene-Treated HeLa Cells
    Sun Y, et al., Acta Biochim Biophys Sin (Shanghai), 47(6):451-8, 2015
    This article characterizes the interaction between Heat shock protein 90 (Hsp90) and its inhibitor nicotinicmycoepoxydiene (NMD). A Pall ForteBio Octet RED system equipped with Super-Streptavidin (SSA) biosensors was used to capture biotinylated Hsp90 binding to NMD. The KD value obtained from the Octet RED system is comparable to that obtained from a Fluorescent assay. Overall results suggest a novel mechanism pertaining to Hsp90 inhibition by NMD.


  • Helicobacter Pylori FlhA Binds the Sensor Kinase and Flagellar Gene Regulatory Protein FlgS with High Affinity
    Tsang J, et al., J Bacteriol, 197(11):1886-92, 2015
    This study provides additional insights into flagellar assembly in Helicobacter pylori. The high affinity interaction between Flagellar Gene Regulatory Protein (Flgs) and FlhA suggest an additional role for FlhA in flagellar assembly. A Pall ForteBio Octet QK system equipped with Streptavidin Biosensor probes was used to capture biotinylated peptides representing residues 1 to 25 of FlhA. The analytes used in this investigation had FlgS or a shorter version called FlgSc.


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